ArticleBiomaterials2016
Utilizing clathrin triskelions as carriers for spatially controlled multi-protein display.
Article in Biomaterials, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- In situ-crosslinked Zippersomes enhance cardiac repair by increasing accumulation and retention.Bioengineering & translational medicine · 2024Article
- Discovery and characterization of a functional scFv for CCR2 inhibition via an extracellular loop.International journal of pharmaceutics · 2023Article
- Rationally designed anisotropic and auxetic hydrogel patches for adaptation to dynamic organs.Advanced functional materials · 2022Article
- Carrier-Free CXCR4-Targeted Nanoplexes Designed for Polarizing Macrophages to Suppress Tumor Growth.Cellular and molecular bioengineering · 2019Article
- Precision engineering of targeted nanocarriers.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2018Review
- Modulating Macrophage Polarization through CCR2 Inhibition and Multivalent Engagement.Molecular pharmaceutics · 2018Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The simultaneous and spatially controlled display of different proteins on nanocarriers is a desirable property not often achieved in practice. Here, we report the use of clathrin triskelions as a versatile platform for functional protein display. We hypothesized that site-specific molecular epitope recognition would allow for effective and ordered protein attachment to clathrin triskelions. Clathrin binding peptides (CBPs) were genetically fused to mCherry and green fluorescent protein (GFP), expressed, and loaded onto clathrin triskelions by site-specific binding. Attachment was confirmed by surface plasmon resonance. mCherry fusion proteins modified with various CBPs displayed binding affinities between 470 nM and 287 μM for the clathrin triskelions. Simultaneous attachment of GFP-Wbox and mCherry-Cbox fusion constructs to the clathrin terminal domain was verified by Förster resonance energy transfer. The circulating half-lives, area under the curve, and the terminal half-lives of GFP and mCherry were significantly increased when attached to clathrin triskelions. Clathrin triskelion technology is useful for the development of versatile and multifunctional carriers for spatially controlled protein or peptide display with tremendous potential in nanotechnology, drug delivery, vaccine development, and targeted therapeutic applications.
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Registered trials
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